Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+) and Organism(s) Rattus norvegicus and UniProt Accession P50170

for references in articles please use BRENDA:EC1.1.1.105
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form . No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3alpha-hydroxysteroids .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P50170
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
all-trans-retinol-[cellular-retinol-binding-protein]
+
=
all-trans-retinal-[cellular-retinol-binding-protein]
+
+
Synonyms
rdh, rdh12, rdh10, dhrs9, retinal reductase, rodh-4, retinol dehydrogenase 12, rdh16, retinol dehydrogenase 10, rdhe2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
all-trans retinol dehydrogenase
-
-
-
-
dehydrogenase, retinol
-
-
-
-
MDR
-
-
-
-
microsomal retinol dehydrogenase
-
-
-
-
P32
-
-
-
-
retinal reductase
-
-
-
-
retinene reductase
-
-
-
-
retinol dehydrogenase (vitamin A1)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
all-trans retinol:NAD+ oxidoreductase
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3alpha-hydroxysteroids [2].
CAS REGISTRY NUMBER
COMMENTARY hide
9033-53-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
show the reaction diagram
retinal + NADH
retinol + NAD+
show the reaction diagram
-
-
-
-
r
retinal + NADPH + H+
retinol + NADP+
show the reaction diagram
retinol + NAD+
retinal + NADH
show the reaction diagram
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chloral hydrate
-
-
Lubrol Px
-
-
sodium deoxycholate
-
-
Triton X-100
-
-
additional information
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BigCHAP
-
10-20% stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
retinol
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
maximal activity at physiological pH
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
80-94% of all enzyme activity
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RDH16_RAT
317
0
35597
Swiss-Prot
Secretory Pathway (Reliability: 2)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing strikingly affects activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of Rdh7
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koen, A.L.; Shaw, C.R.
Retinol and alcohol dehydrogenases in retina and liver
Biochim. Biophys. Acta
128
48-54
1966
Rattus norvegicus
Manually annotated by BRENDA team
Leo, M.A.; Lieber, C.S.
NAD+-dependent retinol dehydrogenase in liver microsomes
Methods Enzymol.
189
520-524
1990
Rattus norvegicus
Manually annotated by BRENDA team
Leo, M.A.; Kim., C.I.; Lieber, C.S.
NAD+-dependent retinol dehydrogenase in liver microsomes
Arch. Biochem. Biophys.
259
241-249
1987
Peromyscus maniculatus, Rattus norvegicus
Manually annotated by BRENDA team
Pares, X.; Farres, J.; Kedishvili, N.; Duester, G.
Medium- and short-chain dehydrogenase/reductase gene and protein families: Medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism
Cell. Mol. Life Sci.
65
3936-3949
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Napoli, J.L.
Physiological insights into all-trans-retinoic acid biosynthesis
Biochim. Biophys. Acta
1821
152-167
2012
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team